2JMX

OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase

Summary for 2JMX

• Entry DOI: 10.2210/pdb2jmx/pdb
• NMR Information: BMRB: 15072
• Descriptor: ATP synthase O subunit, mitochondrial, ATP synthase subunit alpha heart isoform, mitochondrial (2 entities in total)
• Functional Keywords: oscp-nt alpha-nt complex, hydrolase
• Biological source: Bos taurus (cattle); More
• Cellular location: Mitochondrion: P13621; Mitochondrion inner membrane (By similarity): P19483
• Total number of polymer chains: 2
• Total formula weight: 15875.40

Authors

Carbajo, R.J.,Neuhaus, D.,Kellas, F.A.,Yang, J.,Runswick, M.J.,Montgomery, M.G.,Walker, J.E. (deposition date: 2006-12-12, release date: 2007-04-24, Last modification date: 2023-12-20)

Primary citation

Carbajo, R.J.,Kellas, F.A.,Yang, J.-C.,Runswick, M.J.,Montgomery, M.G.,Walker, J.E.,Neuhaus, D.
How the N-terminal Domain of the OSCP Subunit of Bovine F(1)F(o)-ATP Synthase Interacts with the N-terminal Region of an Alpha Subunit
J.Mol.Biol., 368:310-318, 2007

PubMed Abstract: The peripheral stalk of ATP synthase acts as a stator holding the alpha(3)beta(3) catalytic subcomplex and the membrane subunit a against the torque of the rotating central stalk and attached c ring. In bovine mitochondria, the N-terminal domain of the oligomycin sensitivity conferral protein (OSCP-NT; residues 1-120) anchors one end of the peripheral stalk to the N-terminal tails of one or more alpha subunits of the F(1) subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the alpha-peptide.

PubMed: 17355883
DOI: 10.1016/j.jmb.2007.02.059

Experimental method

SOLUTION NMR